From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2j3k.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2j3k.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2j3k| PDB=2j3k | SCENE= }} | | {{STRUCTURE_2j3k| PDB=2j3k | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DOUBLE BOND REDUCTASE (AT5G16970)-TERNARY COMPLEX II'''
| + | ===CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DOUBLE BOND REDUCTASE (AT5G16970)-TERNARY COMPLEX II=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | In this study, we determined the crystal structures of the apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond reductase encoded by At5g16970. This protein, one of 11 homologues in Arabidopsis thaliana, is most closely related to the Pinus taeda phenylpropenal double bond reductase, involved in, for example, heartwood formation. Both enzymes also have essential roles in plant defense, and can function by catalyzing the reduction of the 7-8-double bond of phenylpropanal substrates, such as p-coumaryl and coniferyl aldehydes in vitro. At5g16970 is also capable of reducing toxic substrates with the same alkenal functionality, such as 4-hydroxy-(2E)-nonenal. The overall fold of At5g16970 is similar to that of the zinc-independent medium chain dehydrogenase/reductase superfamily, the members of which have two domains and are dimeric in nature, i.e. in contrast to their original classification as being zinc-containing oxidoreductases. As provisionally anticipated from the kinetic data, the shape of the binding pocket can readily accommodate p-coumaryl aldehyde, coniferyl aldehyde, 4-hydroxy-(2E)-nonenal, and 2-alkenals. However, the enzyme kinetic data among these potential substrates differ, favoring p-coumaryl aldehyde. Tyr-260 is provisionally proposed to function as a general acid/base for hydride transfer. A catalytic mechanism for this reduction, and its applicability to related important detoxification mammalian proteins, is also proposed.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17028190}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17028190 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17028190}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 36: |
Line 40: |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| | [[Category: Ternary complex ii]] | | [[Category: Ternary complex ii]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:16:53 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:07:49 2008'' |
Revision as of 13:07, 28 July 2008
Template:STRUCTURE 2j3k
CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DOUBLE BOND REDUCTASE (AT5G16970)-TERNARY COMPLEX II
Template:ABSTRACT PUBMED 17028190
About this Structure
2J3K is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Mechanistic and structural studies of apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond reductase At5g16970., Youn B, Kim SJ, Moinuddin SG, Lee C, Bedgar DL, Harper AR, Davin LB, Lewis NG, Kang C, J Biol Chem. 2006 Dec 29;281(52):40076-88. Epub 2006 Oct 6. PMID:17028190
Page seeded by OCA on Mon Jul 28 16:07:49 2008
